Metal-containing enzymes and proteins are vital to respiration, metabolism, and energy production. The chemistry of such processes and the biological role of the metal ions are, in most cases, not completely understood. It is the objective of the proposed research to use a variety of spectroscopic methods (including resonance Raman, ultraviolet-visible-near infrared, circular dichroism and electron paramagnetic resonance) to investigate the molecular and electronic structures of the metal-ligand-substrate sites in native and chemically-modified metalloproteins. These studies will be augmented by synthesis and structural characterization of inorganic complexes which may serve as simpler analogs, or models, for the biologically active sites. An understanding of the structural features of the metal coordination sites in metalloproteins will be essential for elucidating the chemical mechanisms of their biological function. BIBLIOGRAPHIC REFERENCES: "A Resonance Raman Study of the Copper Protein Hemocyanin. New Evidence for the Structure of the Oxygen-Binding Site." T.B. Freedman, J.S. Loehr and T.M. Loehr, J. Amer. Chem. Soc., 98, 2809 (1976). "Resonance Raman Spectra of Proteins," T.M. Loehr, J.B.R. Dunn and J.S. Loehr, in "Handbook of Biochemistry and Molecular Biology," 3rd. ed., Vol. III, G.D. Fasman, editor, CRC Press, Cleveland, 1976, pp. 588-92.